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Normal 2‐aminobutyrate oxidation and increased valine oxidation in fibroblasts deficient in pyruvate dehydrogenase
Author(s) -
Borud O.,
Pettersen J. E.
Publication year - 1982
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01799755
Subject(s) - pyruvate dehydrogenase complex , pyruvate decarboxylation , valine , pyruvate dehydrogenase phosphatase , alanine , dihydrolipoyl transacetylase , pyruvate dehydrogenase kinase , biochemistry , leucine , dehydrogenase , butyric acid , branched chain alpha keto acid dehydrogenase complex , oxoglutarate dehydrogenase complex , chemistry , amino acid , pyruvic acid , enzyme , biology
Human skin fibroblasts deficient in pyruvate dehydrogenase and five normal control strains were incubated with one of the following labelled substrates: dl ‐[1‐ 14 C]‐2‐amino‐n‐butyric acid, dl ‐[3‐ 14 C]‐2‐amino‐n‐butyric acid, dl ‐[1‐ 14 C]leucine, l ‐[1‐ 14 C]valine, l ‐[1‐ 14 C]alanine, and [1‐ 14 C]pyruvate. The rate of 14 CO 2 ‐production in the deficient cells was normal from 2‐aminobutyrate and leucine, increased from valine, and decreased from alanine and pyruvate. These results indicated that in human skin fibroblasts the decarboxylation of 2‐oxobutyrate is catalysed by an enzyme system different from the pyruvate dehydrogenase complex.